7kq3 | pdb_00007kq3

Structure of isethionate sulfite-lyase from Bilophila wadsworthia with substrate isethionate bound

spinqualitylabelsall models 7kq3, resolution 2.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7kq3 is a 4 chain structure with sequence from Bilophila wadsworthia 3_1_6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.688Å Ligands: 8X3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ISLA_BILW3 Involved in an anaerobic respiration pathway that converts the sulfonate taurine (2-aminoethanesulfonate) to ammonia, acetate and sulfide. Catalyzes the radical-mediated C-S bond cleavage of isethionate (2-hydroxyethanesulfonate) to form sulfite and acetaldehyde. Is not able to use any alternate organosulfonate or (S)-1,2-propanediol or choline as a substrate, showing that this enzyme is highly specific for isethionate. Publication Abstract from PubMed Desulfonation of isethionate by the bacterial glycyl radical enzyme (GRE) isethionate sulfite-lyase (IslA) generates sulfite, a substrate for respiration that in turn produces the disease-associated metabolite hydrogen sulfide. Here, we present a 2.7 A resolution X-ray structure of wild-type IslA from Bilophila wadsworthia with isethionate bound. In comparison with other GREs, alternate positioning of the active site beta strands allows for distinct residue positions to contribute to substrate binding. These structural differences, combined with sequence variations, create a highly tailored active site for the binding of the negatively charged isethionate substrate. Through the kinetic analysis of 14 IslA variants and computational analyses, we probe the mechanism by which radical chemistry is used for C-S bond cleavage. This work further elucidates the structural basis of chemistry within the GRE superfamily and will inform structure-based inhibitor design of IsIA and thus of microbial hydrogen sulfide production. Molecular basis of C-S bond cleavage in the glycyl radical enzyme isethionate sulfite-lyase.,Dawson CD, Irwin SM, Backman LRF, Le C, Wang JX, Vennelakanti V, Yang Z, Kulik HJ, Drennan CL, Balskus EP Cell Chem Biol. 2021 Mar 19. pii: S2451-9456(21)00110-0. doi:, 10.1016/j.chembiol.2021.03.001. PMID:33773110 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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